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- PDB-7tn0: SARS-CoV-2 Omicron RBD in complex with human ACE2 and S304 Fab an... -

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Basic information

Entry
Database: PDB / ID: 7tn0
TitleSARS-CoV-2 Omicron RBD in complex with human ACE2 and S304 Fab and S309 Fab
Components
  • Angiotensin-converting enzyme 2
  • S304 Fab heavy chain
  • S304 Fab light chain
  • S309 heavy chain
  • S309 light chain
  • Spike protein S1
KeywordsVIRAL PROTEIN/IMMUNE SYSTEM / COVID-19 / SARS-CoV-2 / neutralizing monoclonal antibody / SARS-CoV-2 receptor human ACE2 / VIRAL PROTEIN-IMMUNE SYSTEM complex / Structural Genomics / Seattle Structural Genomics Center for Infectious Disease / SSGCID
Function / homology
Function and homology information


positive regulation of amino acid transport / angiotensin-converting enzyme 2 / positive regulation of L-proline import across plasma membrane / Hydrolases; Acting on peptide bonds (peptidases); Metallocarboxypeptidases / angiotensin-mediated drinking behavior / regulation of systemic arterial blood pressure by renin-angiotensin / tryptophan transport / positive regulation of gap junction assembly / regulation of vasoconstriction / regulation of cardiac conduction ...positive regulation of amino acid transport / angiotensin-converting enzyme 2 / positive regulation of L-proline import across plasma membrane / Hydrolases; Acting on peptide bonds (peptidases); Metallocarboxypeptidases / angiotensin-mediated drinking behavior / regulation of systemic arterial blood pressure by renin-angiotensin / tryptophan transport / positive regulation of gap junction assembly / regulation of vasoconstriction / regulation of cardiac conduction / peptidyl-dipeptidase activity / maternal process involved in female pregnancy / angiotensin maturation / metallocarboxypeptidase activity / Metabolism of Angiotensinogen to Angiotensins / Attachment and Entry / carboxypeptidase activity / negative regulation of signaling receptor activity / positive regulation of cardiac muscle contraction / regulation of cytokine production / viral life cycle / blood vessel diameter maintenance / brush border membrane / regulation of transmembrane transporter activity / negative regulation of smooth muscle cell proliferation / negative regulation of ERK1 and ERK2 cascade / cilium / metallopeptidase activity / endocytic vesicle membrane / positive regulation of reactive oxygen species metabolic process / virus receptor activity / regulation of cell population proliferation / regulation of inflammatory response / Maturation of spike protein / viral translation / Translation of Structural Proteins / Virion Assembly and Release / endopeptidase activity / host cell surface / host extracellular space / suppression by virus of host tetherin activity / Induction of Cell-Cell Fusion / Potential therapeutics for SARS / structural constituent of virion / host cell endoplasmic reticulum-Golgi intermediate compartment membrane / entry receptor-mediated virion attachment to host cell / receptor-mediated endocytosis of virus by host cell / Attachment and Entry / membrane fusion / positive regulation of viral entry into host cell / receptor-mediated virion attachment to host cell / receptor ligand activity / host cell surface receptor binding / symbiont entry into host cell / membrane raft / apical plasma membrane / fusion of virus membrane with host plasma membrane / endoplasmic reticulum lumen / fusion of virus membrane with host endosome membrane / viral envelope / virion attachment to host cell / SARS-CoV-2 activates/modulates innate and adaptive immune responses / host cell plasma membrane / virion membrane / cell surface / extracellular space / extracellular exosome / zinc ion binding / extracellular region / membrane / identical protein binding / plasma membrane
Similarity search - Function
Collectrin-like domain profile. / Collectrin domain / Renal amino acid transporter / Peptidase family M2 domain profile. / Peptidase M2, peptidyl-dipeptidase A / Angiotensin-converting enzyme / Neutral zinc metallopeptidases, zinc-binding region signature. / Spike (S) protein S1 subunit, receptor-binding domain, SARS-CoV-2 / Spike (S) protein S1 subunit, N-terminal domain, SARS-CoV-like / Betacoronavirus spike (S) glycoprotein S1 subunit N-terminal (NTD) domain profile. ...Collectrin-like domain profile. / Collectrin domain / Renal amino acid transporter / Peptidase family M2 domain profile. / Peptidase M2, peptidyl-dipeptidase A / Angiotensin-converting enzyme / Neutral zinc metallopeptidases, zinc-binding region signature. / Spike (S) protein S1 subunit, receptor-binding domain, SARS-CoV-2 / Spike (S) protein S1 subunit, N-terminal domain, SARS-CoV-like / Betacoronavirus spike (S) glycoprotein S1 subunit N-terminal (NTD) domain profile. / Spike glycoprotein, N-terminal domain superfamily / Betacoronavirus spike (S) glycoprotein S1 subunit C-terminal (CTD) domain profile. / Spike glycoprotein, betacoronavirus / Spike (S) protein S1 subunit, receptor-binding domain, betacoronavirus / Spike S1 subunit, receptor binding domain superfamily, betacoronavirus / Betacoronavirus spike glycoprotein S1, receptor binding / Spike glycoprotein S1, N-terminal domain, betacoronavirus-like / Betacoronavirus-like spike glycoprotein S1, N-terminal / Spike glycoprotein S2, coronavirus, heptad repeat 1 / Spike glycoprotein S2, coronavirus, heptad repeat 2 / Coronavirus spike (S) glycoprotein S2 subunit heptad repeat 2 (HR2) region profile. / Coronavirus spike (S) glycoprotein S2 subunit heptad repeat 1 (HR1) region profile. / Spike glycoprotein S2 superfamily, coronavirus / Spike glycoprotein S2, coronavirus / Coronavirus spike glycoprotein S2 / Coronavirus spike glycoprotein S1, C-terminal / Coronavirus spike glycoprotein S1, C-terminal
Similarity search - Domain/homology
Spike glycoprotein / Angiotensin-converting enzyme 2
Similarity search - Component
Biological speciesHomo sapiens (human)
Severe acute respiratory syndrome coronavirus 2
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.85 Å
AuthorsMcCallum, M. / Czudnochowski, N. / Nix, J.C. / Croll, T.I. / SSGCID / Dillen, J.R. / Snell, G. / Veesler, D. / Seattle Structural Genomics Center for Infectious Disease (SSGCID)
Funding support1items
OrganizationGrant numberCountry
Not funded
CitationJournal: Science / Year: 2022
Title: Structural basis of SARS-CoV-2 Omicron immune evasion and receptor engagement.
Authors: Matthew McCallum / Nadine Czudnochowski / Laura E Rosen / Samantha K Zepeda / John E Bowen / Alexandra C Walls / Kevin Hauser / Anshu Joshi / Cameron Stewart / Josh R Dillen / Abigail E ...Authors: Matthew McCallum / Nadine Czudnochowski / Laura E Rosen / Samantha K Zepeda / John E Bowen / Alexandra C Walls / Kevin Hauser / Anshu Joshi / Cameron Stewart / Josh R Dillen / Abigail E Powell / Tristan I Croll / Jay Nix / Herbert W Virgin / Davide Corti / Gyorgy Snell / David Veesler /
Abstract: The severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) Omicron variant of concern evades antibody-mediated immunity that comes from vaccination or infection with earlier variants due to ...The severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) Omicron variant of concern evades antibody-mediated immunity that comes from vaccination or infection with earlier variants due to accumulation of numerous spike mutations. To understand the Omicron antigenic shift, we determined cryo-electron microscopy and x-ray crystal structures of the spike protein and the receptor-binding domain bound to the broadly neutralizing sarbecovirus monoclonal antibody (mAb) S309 (the parent mAb of sotrovimab) and to the human ACE2 receptor. We provide a blueprint for understanding the marked reduction of binding of other therapeutic mAbs that leads to dampened neutralizing activity. Remodeling of interactions between the Omicron receptor-binding domain and human ACE2 likely explains the enhanced affinity for the host receptor relative to the ancestral virus.
History
DepositionJan 20, 2022Deposition site: RCSB / Processing site: RCSB
Revision 1.0Feb 2, 2022Provider: repository / Type: Initial release
Revision 1.1Feb 9, 2022Group: Database references / Category: citation / citation_author
Item: _citation.journal_volume / _citation.page_first ..._citation.journal_volume / _citation.page_first / _citation.page_last / _citation.pdbx_database_id_PubMed / _citation.title / _citation_author.identifier_ORCID
Revision 1.2Feb 16, 2022Group: Other / Structure summary
Category: audit_author / pdbx_SG_project ...audit_author / pdbx_SG_project / pdbx_database_status / struct_keywords
Item: _pdbx_database_status.SG_entry / _struct_keywords.text
Revision 1.3Mar 9, 2022Group: Database references / Category: citation / citation_author
Item: _citation.journal_volume / _citation.page_first ..._citation.journal_volume / _citation.page_first / _citation.page_last / _citation_author.identifier_ORCID
Revision 1.4Oct 18, 2023Group: Data collection / Refinement description
Category: chem_comp_atom / chem_comp_bond / pdbx_initial_refinement_model

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: S309 light chain
B: S309 heavy chain
C: S309 heavy chain
D: S309 light chain
E: Angiotensin-converting enzyme 2
F: Angiotensin-converting enzyme 2
G: S304 Fab light chain
H: S304 Fab heavy chain
I: Spike protein S1
M: S304 Fab heavy chain
N: S304 Fab light chain
S: Spike protein S1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)382,45957
Polymers378,46712
Non-polymers3,99145
Water3,369187
1
A: S309 light chain
B: S309 heavy chain
E: Angiotensin-converting enzyme 2
G: S304 Fab light chain
H: S304 Fab heavy chain
I: Spike protein S1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)191,26528
Polymers189,2346
Non-polymers2,03122
Water1086
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
C: S309 heavy chain
D: S309 light chain
F: Angiotensin-converting enzyme 2
M: S304 Fab heavy chain
N: S304 Fab light chain
S: Spike protein S1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)191,19429
Polymers189,2346
Non-polymers1,96023
Water905
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)78.280, 183.650, 194.550
Angle α, β, γ (deg.)90.000, 95.980, 90.000
Int Tables number4
Space group name H-MP1211
Space group name HallP2yb
Symmetry operation#1: x,y,z
#2: -x,y+1/2,-z

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Components

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Protein , 2 types, 4 molecules EFIS

#3: Protein Angiotensin-converting enzyme 2 /


Mass: 69620.273 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: ACE2, UNQ868/PRO1885 / Production host: Cricetulus griseus (Chinese hamster) / References: UniProt: Q9BYF1
#6: Protein Spike protein S1


Mass: 24735.871 Da / Num. of mol.: 2 / Fragment: Receptor-binding domain
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Severe acute respiratory syndrome coronavirus 2
Gene: S, 2 / Production host: Homo sapiens (human) / References: UniProt: P0DTC2

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Antibody , 4 types, 8 molecules ADBCGNHM

#1: Antibody S309 light chain


Mass: 23204.697 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Cell line (production host): HEK293 suspension / Production host: Homo sapiens (human)
#2: Antibody S309 heavy chain


Mass: 24573.471 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Cell line (production host): HEK293 suspension / Production host: Homo sapiens (human)
#4: Antibody S304 Fab light chain


Mass: 23369.947 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Cell line (production host): HEK293 suspension / Production host: Homo sapiens (human)
#5: Antibody S304 Fab heavy chain


Mass: 23729.389 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Cell line (production host): HEK293 suspension / Production host: Homo sapiens (human)

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Sugars , 1 types, 11 molecules

#10: Sugar
ChemComp-NAG / 2-acetamido-2-deoxy-beta-D-glucopyranose / N-acetyl-beta-D-glucosamine / 2-acetamido-2-deoxy-beta-D-glucose / 2-acetamido-2-deoxy-D-glucose / 2-acetamido-2-deoxy-glucose / N-ACETYL-D-GLUCOSAMINE / N-Acetylglucosamine


Type: D-saccharide, beta linking / Mass: 221.208 Da / Num. of mol.: 11 / Source method: isolated from a natural source / Formula: C8H15NO6
IdentifierTypeProgram
DGlcpNAcbCONDENSED IUPAC CARBOHYDRATE SYMBOLGMML 1.0
N-acetyl-b-D-glucopyranosamineCOMMON NAMEGMML 1.0
b-D-GlcpNAcIUPAC CARBOHYDRATE SYMBOLPDB-CARE 1.0
GlcNAcSNFG CARBOHYDRATE SYMBOLGMML 1.0

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Non-polymers , 4 types, 221 molecules

#7: Chemical
ChemComp-EDO / 1,2-ETHANEDIOL / ETHYLENE GLYCOL / Ethylene glycol


Mass: 62.068 Da / Num. of mol.: 11 / Source method: obtained synthetically / Formula: C2H6O2
#8: Chemical...
ChemComp-CL / CHLORIDE ION / Chloride


Mass: 35.453 Da / Num. of mol.: 21 / Source method: obtained synthetically / Formula: Cl
#9: Chemical ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Formula: Zn
#11: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 187 / Source method: isolated from a natural source / Formula: H2O

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Details

Has ligand of interestN

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 1

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Sample preparation

CrystalDensity Matthews: 3.82 Å3/Da / Density % sol: 67.79 %
Crystal growTemperature: 293.15 K / Method: vapor diffusion, sitting drop
Details: 20% v/v Ethylene glycol, 10% w/v PEG 8000, 0.1 M Tris (base)/BICINE pH 8.5, 0.1 M NDSB-256

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: ALS / Beamline: 4.2.2 / Wavelength: 1.07216 Å
DetectorType: RDI CMOS_8M / Detector: CMOS / Date: Dec 23, 2021
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.07216 Å / Relative weight: 1
ReflectionResolution: 2.85→48.91 Å / Num. obs: 121127 / % possible obs: 96.7 % / Redundancy: 5.8 % / Biso Wilson estimate: 53.45 Å2 / CC1/2: 0.975 / Net I/σ(I): 5.6
Reflection shellResolution: 2.85→2.9 Å / Num. unique obs: 6212 / CC1/2: 0.209

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Processing

Software
NameVersionClassification
PHENIX1.20_4459refinement
PHENIX1.20_4459refinement
XDSdata reduction
Aimlessdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 7JX3

7jx3


Resolution: 2.85→48.91 Å / SU ML: 0.4499 / Cross valid method: FREE R-VALUE / σ(F): 1.34 / Phase error: 28.9166
Stereochemistry target values: GeoStd + Monomer Library + CDL v1.2
RfactorNum. reflection% reflection
Rfree0.2679 6055 5 %
Rwork0.2303 115072 -
obs0.2322 121127 95.17 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.1 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso mean: 63.5 Å2
Refinement stepCycle: LAST / Resolution: 2.85→48.91 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms24463 0 221 187 24871
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00325291
X-RAY DIFFRACTIONf_angle_d0.657634495
X-RAY DIFFRACTIONf_chiral_restr0.04483835
X-RAY DIFFRACTIONf_plane_restr0.00454479
X-RAY DIFFRACTIONf_dihedral_angle_d11.86978661
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.85-2.880.39372050.34683618X-RAY DIFFRACTION89.85
2.88-2.920.35742040.34153589X-RAY DIFFRACTION90.42
2.92-2.950.37491860.32923713X-RAY DIFFRACTION92.77
2.95-2.990.36922040.31163779X-RAY DIFFRACTION93.56
2.99-3.030.37072130.31843869X-RAY DIFFRACTION95.78
3.03-3.070.34112190.30023799X-RAY DIFFRACTION95.96
3.07-3.110.36061940.30993920X-RAY DIFFRACTION96.82
3.11-3.160.34572110.30443907X-RAY DIFFRACTION97.31
3.16-3.210.33231960.29443923X-RAY DIFFRACTION97.49
3.21-3.260.33522020.28953963X-RAY DIFFRACTION97.36
3.26-3.320.33271900.27583843X-RAY DIFFRACTION97.09
3.32-3.380.32191960.26853937X-RAY DIFFRACTION97.43
3.38-3.440.30462160.26473895X-RAY DIFFRACTION96.8
3.44-3.510.29732210.25823884X-RAY DIFFRACTION97.25
3.51-3.590.30332150.25313897X-RAY DIFFRACTION96.89
3.59-3.670.30232160.24393887X-RAY DIFFRACTION96.77
3.67-3.770.28241920.23883914X-RAY DIFFRACTION96.77
3.77-3.870.27731800.23693883X-RAY DIFFRACTION96.46
3.87-3.980.26161980.21333883X-RAY DIFFRACTION96.36
3.98-4.110.24742030.19823900X-RAY DIFFRACTION96
4.11-4.260.24072140.19163820X-RAY DIFFRACTION95.91
4.26-4.430.22682060.18523855X-RAY DIFFRACTION95.6
4.43-4.630.2291930.18333902X-RAY DIFFRACTION95.41
4.63-4.870.22642040.17593815X-RAY DIFFRACTION95.15
4.87-5.180.22141570.19193863X-RAY DIFFRACTION94.72
5.18-5.580.22121920.20053850X-RAY DIFFRACTION94.44
5.58-6.140.23512040.21373770X-RAY DIFFRACTION94.17
6.14-7.020.25251920.21663797X-RAY DIFFRACTION93.35
7.02-8.840.21092210.19723749X-RAY DIFFRACTION92.48
8.84-48.910.1962110.18883648X-RAY DIFFRACTION88.96
Refinement TLS params.

Method: refined / Refine-ID: X-RAY DIFFRACTION

IDL11 (°2)L12 (°2)L13 (°2)L22 (°2)L23 (°2)L33 (°2)S11 (Å °)S12 (Å °)S13 (Å °)S21 (Å °)S22 (Å °)S23 (Å °)S31 (Å °)S32 (Å °)S33 (Å °)T11 (Å2)T12 (Å2)T13 (Å2)T22 (Å2)T23 (Å2)T33 (Å2)Origin x (Å)Origin y (Å)Origin z (Å)
11.515896672520.0428312367787-0.7458745425461.815761797670.6929122891842.941615051920.1840269100090.1185720881540.381754235707-0.0880152827873-0.0843014226065-0.195358136412-0.3577840933420.109491869885-0.05387856295690.424456348914-0.04556956917590.005510367593040.3328838853130.1366244576410.38869791996415.097-14.327142.438
21.88923252270.503640018289-0.5486322792982.62765039026-1.388438866152.977622018030.123673447941-0.3288751420370.295809546271-0.0409744721955-0.07951162256070.07833013465210.12170495088-0.0582719245323-0.0995126782670.299496368716-0.0311365673419-0.02944114151870.329437200758-0.07908483055770.3338867466872.275-22.793174.671
31.165430050630.764449947782-0.7901082865251.573661308990.06684184042562.30321980318-0.1630538549260.132071793316-0.0480744527077-0.11033113678-0.03314313264370.01036254569840.384556879044-0.04877728090470.2009884701750.429399861658-0.073957344096-0.01304282416310.2978002454750.08497697526510.3367213350156.99-33.812135.422
42.58869781855-0.394553507864-0.3444291060941.65343810356-0.3199911488992.58478824315-0.0018801913294-0.07249966600270.114426896763-0.0831662912577-0.03749450992320.08839156547530.173364835684-0.5936626085320.02022646535360.331483057803-0.0554879828594-0.04534915875180.3800541802950.01366286674180.389788352976-10.423-26.128164.928
51.720006366310.308513381877-0.1325491419991.814106563230.333744909021.057525292590.0952639337288-0.3593673326140.8921387237630.00824359986522-0.0148313820990.0316553643224-0.4146690532350.357370530319-0.0326705554790.567366145789-0.2086200080650.04515142780080.778047171866-0.03727174089410.84646887535152.12916.214116.533
61.904285005680.659796155858-0.8701993129312.1767862973-0.5472764574522.698919279840.1628462724750.05187079032260.03441222866090.0216729102970.09716607769690.221313192090.310604938511-0.0804585053236-0.2034849994680.327451949932-0.00107408197818-0.04915653745470.3491607943160.07459964619790.30480129793516.958-6.12880.032
71.48036903481-0.170821264215-0.1329559354691.297658569330.6223137388531.692821750850.3242124808770.02127513690790.735548636784-0.2448293443270.148836895849-0.030684728772-0.806814954799-0.363190004978-0.3771186925190.7874281466780.1593994762710.224090156360.5556902556590.2327218876750.80207189511812.57129.01169.229
81.78455674618-0.342076532913-0.1537647656273.21026546234-0.3142773712262.817940153290.109288559508-0.4984985453880.01730008678170.2875496587920.05375665284740.0120215824802-0.157052379642-0.350354017378-0.1057408389160.364610971266-0.06830047565390.04509778394150.5365212838620.06337836163760.3233543864546.3740.59697.57
91.59167557534-0.2693354718180.2793012582021.89004897235-0.6119181876563.739633041830.2924161210730.1254124502890.4461315773250.005118969630370.07080833620250.503063379536-0.526398766049-1.19704833325-0.373504883920.5347055289550.1911121322870.08879540769640.8204436320650.09364710019360.5757693352010.71724.28779.325
102.274672513760.7352079298810.3384932634941.370974409750.0621555570661.798611869030.03488030433270.0554431882746-0.0455264956513-0.0523781231735-0.0471832054410.000534388466730.3409742005970.057509562777-0.005354686387070.442356031014-0.0190973770254-0.00503127111390.4780652528290.1860894624610.33471900188327.537-20.477110.046
111.738904590470.269388039575-1.352425550811.35357224606-1.20589641323.109175440880.262805088586-0.0156329302340.2431878579480.09856855800720.0492040923063-0.0110328929515-0.12900699289-0.0240230644755-0.2813454077750.3773580446910.0705183808193-0.02112935906190.356424860565-0.1329166930940.34829246128535.47-16.5162.308
121.685564799140.382003484215-0.4111019092542.392714970040.6488526999873.594784591920.02251436842610.01767346414280.2384057723020.02955252903890.0767443359871-0.09201332308970.3544625808270.475365134049-0.08797069116560.262605900930.0465937033223-0.02367781566830.3669342768540.04564696696450.33543104383548.006-22.966-30.281
131.5884743669-0.734827894685-1.276908493641.26924647884-0.7160249480452.91071630795-0.0898331983350.00561010953093-0.245945278848-0.102722858132-0.104285846877-0.1376228410750.7039462270750.2393489891360.179417847780.5343023487110.130038265286-0.04031402398860.402627830867-0.09374581678030.44098223119743.022-36.6148.276
142.234425811110.808332374928-0.6029366025222.003216849840.02562553112781.41659989252-0.0733584880312-0.03057469108140.1377583400730.0791324264405-0.0209173221436-0.1571693744580.3885042377360.4681222220480.1392500094180.4502481434150.174925530354-0.05324476777120.623884102224-0.09895260444540.47587906829760.826-27.304-21.906
150.76439644963-0.7054337929150.07366953878082.06456405102-0.1374591374940.2983861985440.01794658353450.186803409380.0302742960157-0.209699912674-0.0721576720024-0.149289087861-0.0350531699929-0.06833181289990.05905513163760.3638531598440.00843603750245-0.0311207018360.421686819581-0.04895499192120.364446812591-3.1816.60924.503
161.09954755215-0.670330146759-1.230592869062.473376596511.318177737182.664025738740.0323416604117-0.118804198283-0.1735924394-0.0334150203272-0.07834164346910.1314156710090.1200528674830.02824763003010.07271987059050.237961695283-0.0314270595001-0.06205378865530.2676979416240.07314933437890.26619194438233.528-6.8862.889
171.455063174440.814460732421-0.08861536970483.51360961441-1.600243959432.176129158190.0380532040236-0.05468922873740.3692034251290.3879454353540.186120190788-0.0233099123662-0.456337460242-0.252298973033-0.2329664676570.607117977361-0.03657236043610.01516334411050.404237261771-0.02282839930370.39131489962237.37829.10370.782
182.25485856164-0.0593313739494-0.8469847651563.257429446720.4702788152331.770530623010.04844140370450.284367843496-0.0690088566532-0.332165929005-0.015946284762-0.0651062650799-0.3041717789940.129615463416-0.01242951832290.314124228655-0.00245813088808-0.008861278179990.367686858482-0.01528320212550.20134618009544.033-1.37944.778
191.711249477430.1708482148140.4682936955032.04089570295-0.4783887866372.33903472018-0.03470883775990.05532412090960.125287912024-0.335245652116-0.107621327456-0.3900176532860.1044131988850.4838771377970.1182401260410.519017305047-0.02602066523090.1170504112250.4453405131580.09571166161380.36995012015149.65123.51361.627
202.66287601691-1.16645128930.4356603193541.04952491335-0.2835730836811.961053431960.09158284036230.0512689371013-0.142882701924-0.0186895693225-0.1846685728640.1045793638820.161633406209-0.0529071349680.09713258603830.43590868344-0.0179014852537-0.0282857583220.274059696893-0.07996954279950.41756865405122.816-23.15233.518
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1( CHAIN D AND RESID 1:108 )D1 - 108
2X-RAY DIFFRACTION2( CHAIN D AND RESID 109:214 )D109 - 214
3X-RAY DIFFRACTION3( CHAIN C AND RESID 1:127 )C1 - 127
4X-RAY DIFFRACTION4( CHAIN C AND RESID 128:228 )C128 - 228
5X-RAY DIFFRACTION5( CHAIN F AND RESID 19:602 )F19 - 602
6X-RAY DIFFRACTION6( CHAIN N AND RESID 1:108 )N1 - 108
7X-RAY DIFFRACTION7( CHAIN N AND RESID 109:214 )N109 - 214
8X-RAY DIFFRACTION8( CHAIN M AND RESID 1:120 )M1 - 120
9X-RAY DIFFRACTION9( CHAIN M AND RESID 121:220 )M121 - 220
10X-RAY DIFFRACTION10( CHAIN S AND RESID 331:529 )S331 - 529
11X-RAY DIFFRACTION11( CHAIN A AND RESID 1:108 )A1 - 108
12X-RAY DIFFRACTION12( CHAIN A AND RESID 109:213 )A109 - 213
13X-RAY DIFFRACTION13( CHAIN B AND RESID 1:127 )B1 - 127
14X-RAY DIFFRACTION14( CHAIN B AND RESID 128:228 )B128 - 228
15X-RAY DIFFRACTION15( CHAIN E AND RESID 19:613 )E19 - 613
16X-RAY DIFFRACTION16( CHAIN G AND RESID 1:108 )G1 - 108
17X-RAY DIFFRACTION17( CHAIN G AND RESID 109:214 )G109 - 214
18X-RAY DIFFRACTION18( CHAIN H AND RESID 1:120 )H1 - 120
19X-RAY DIFFRACTION19( CHAIN H AND RESID 121:220 )H121 - 220
20X-RAY DIFFRACTION20( CHAIN I AND RESID 332:529 )I332 - 529

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